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Research Article Free access | 10.1172/JCI110706

Association of hemoglobin C with erythrocyte ghosts.

G H Reiss, H M Ranney, and N Shaklai

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Published November 1, 1982 - More info

Published in Volume 70, Issue 5 on November 1, 1982
J Clin Invest. 1982;70(5):946–952. https://doi.org/10.1172/JCI110706.
© 1982 The American Society for Clinical Investigation
Published November 1, 1982 - Version history
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Abstract

The interaction of hemoglobin C (Hb C) with erythrocyte membranes was studied using changes in fluorescence intensity in a membrane-embedded probe. The affinity of Hb C for the membranes at pH 6.0 and pH 6.8 was compared to that of normal hemoglobin (Hb A). Steady-state and kinetic data were delivered. The affinity of Hb C for the erythrocyte membrane at pH 6.8 appeared to be about five times greater than that of Hb A. The associations of Hb C and Hb A with the membrane were reversible to about the same extent. The cytoplasmic portions of band 3 membrane proteins were suggested to be the binding sites for both hemoglobins. The membrane binding of Hb C at pH values of 6.8 to 7.0 indicates that this reaction may occur under physiological circumstances.

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